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Protein

Lead, cadmium, zinc and mercury-transporting ATPase

Gene

zntA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in export of lead, cadmium, zinc and mercury.

Catalytic activityi

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).
ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Zinc
Metal bindingi59 – 591Zinc
Metal bindingi62 – 621Zinc
Active sitei436 – 43614-aspartylphosphate intermediateBy similarity
Metal bindingi628 – 6281MagnesiumPROSITE-ProRule annotation
Metal bindingi632 – 6321MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: EcoliWiki
  • ATP binding Source: UniProtKB-KW
  • cadmium-exporting ATPase activity Source: EcoCyc
  • cobalt ion transmembrane transporter activity Source: EcoCyc
  • lead ion transmembrane transporter activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • nickel cation transmembrane transporter activity Source: EcoCyc
  • zinc-exporting ATPase activity Source: EcoCyc

GO - Biological processi

  • cadmium ion transmembrane transport Source: GOC
  • cobalt ion transport Source: EcoCyc
  • detoxification of zinc ion Source: EcoliWiki
  • lead ion transport Source: EcoCyc
  • nickel cation transmembrane transport Source: GOC
  • response to cadmium ion Source: EcoliWiki
  • zinc II ion transmembrane transport Source: GOC
  • zinc II ion transport Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Cadmium, Magnesium, Mercury, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RKP37617.

Protein family/group databases

TCDBi3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Lead, cadmium, zinc and mercury-transporting ATPase (EC:3.6.3.3, EC:3.6.3.5)
Gene namesi
Name:zntA
Synonyms:yhhO
Ordered Locus Names:b3469, JW3434
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12215. zntA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence AnalysisAdd
BLAST
Topological domaini146 – 19146CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei192 – 21221HelicalSequence AnalysisAdd
BLAST
Topological domaini213 – 356144PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei357 – 37721HelicalSequence AnalysisAdd
BLAST
Topological domaini378 – 3836CytoplasmicSequence Analysis
Transmembranei384 – 40421HelicalSequence AnalysisAdd
BLAST
Topological domaini405 – 46157PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei462 – 48221HelicalSequence AnalysisAdd
BLAST
Topological domaini483 – 632150CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei633 – 65321HelicalSequence AnalysisAdd
BLAST
Topological domaini654 – 69340PeriplasmicSequence AnalysisAdd
BLAST
Transmembranei694 – 71421HelicalSequence AnalysisAdd
BLAST
Topological domaini715 – 73218CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Lead, cadmium, zinc and mercury-transporting ATPasePRO_0000046332Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP37617.
PRIDEiP37617.

Interactioni

Protein-protein interaction databases

DIPiDIP-12947N.
IntActiP37617. 8 interactions.
MINTiMINT-1256950.
STRINGi511145.b3469.

Structurei

Secondary structure

1
732
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 569Combined sources
Helixi62 – 7110Combined sources
Beta strandi73 – 8210Combined sources
Turni83 – 864Combined sources
Beta strandi87 – 948Combined sources
Helixi97 – 10711Combined sources
Beta strandi110 – 1134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
ProteinModelPortaliP37617.
SMRiP37617. Positions 46-118, 126-730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37617.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 11365HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250399.
InParanoidiP37617.
KOiK01534.
OMAiPAMKAST.
OrthoDBiEOG6742RM.
PhylomeDBiP37617.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY
60 70 80 90 100
SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV
110 120 130 140 150
ESALQKAGYS LRDEQAAEEP QASRLKENLP LITLIVMMAI SWGLEQFNHP
160 170 180 190 200
FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT
210 220 230 240 250
AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRKGEREEV
260 270 280 290 300
AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD
310 320 330 340 350
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF
360 370 380 390 400
SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST
410 420 430 440 450
PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA
460 470 480 490 500
IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA
510 520 530 540 550
LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ TVVLVVRNDD
560 570 580 590 600
VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
610 620 630 640 650
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD
660 670 680 690 700
VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT
710 720 730
LLGMTGLWLA VLADTGATVL VTANALRLLR RR
Length:732
Mass (Da):76,840
Last modified:October 1, 1994 - v1
Checksum:i25476EA830786465
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.
PIRiS47688.
RefSeqiNP_417926.1. NC_000913.3.
WP_000106551.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.
GeneIDi947972.
KEGGieco:b3469.
PATRICi32122382. VBIEscCol129921_3568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.
PIRiS47688.
RefSeqiNP_417926.1. NC_000913.3.
WP_000106551.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
ProteinModelPortaliP37617.
SMRiP37617. Positions 46-118, 126-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-12947N.
IntActiP37617. 8 interactions.
MINTiMINT-1256950.
STRINGi511145.b3469.

Protein family/group databases

TCDBi3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiP37617.
PRIDEiP37617.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.
GeneIDi947972.
KEGGieco:b3469.
PATRICi32122382. VBIEscCol129921_3568.

Organism-specific databases

EchoBASEiEB2129.
EcoGeneiEG12215. zntA.

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250399.
InParanoidiP37617.
KOiK01534.
OMAiPAMKAST.
OrthoDBiEOG6742RM.
PhylomeDBiP37617.

Enzyme and pathway databases

BioCyciEcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RKP37617.

Miscellaneous databases

EvolutionaryTraceiP37617.
PROiP37617.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase."
    Rensing C., Mitra B., Rosen B.P.
    Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase."
    Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K.
    Mol. Microbiol. 25:883-891(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli."
    Sharma R., Rensing C., Rosen B.P., Mitra B.
    J. Biol. Chem. 275:3873-3878(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)."
    Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V.
    J. Mol. Biol. 323:883-897(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.

Entry informationi

Entry nameiATZN_ECOLI
AccessioniPrimary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 22, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.